Structural Basis for the Recognition of Blood Group Trisaccharides by Norovirus

Cao, Sheng; Lou, Zhiyong; Tan, Ming; Chen, Yutao; Liu, Yijin; Zhang, Zhushan; Zhang, Xuejun C.; Jiang, Xi; Li, Xuemei; Rao, Zihe

doi:10.1128/jvi.00219-07

Cited by 340 publications

(479 citation statements)

References 32 publications

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“…When comparing the potential trisaccharide A and B interacting positions (343-345 and 374) (Cao et al, 2007), we found residues 344 (Val), 345 (Phe) and 374 (Pro) to be ACR in all partitions, and residue 343 to be class-specific from partition II to partition X. A second plausible binding pocket (except from the one located in the domain interface) includes residues 390-392, 395 and 344 (Cao et al, 2007).…”

Section: Discussionmentioning

confidence: 99%

“…Cao and coworkers have previously proposed from crystal structure studies that residues involved in binding of A and B trisaccharide to the P2 domain of GII.4 virus (VA387 strain), located at the dimer interface, are 343 (Ser), 344 (Thr), 345 (Arg) and 374 (Asp) from one protomer and 441 (Ser), 442 (Gly) and 443 (Tyr) in the other (Cao et al, 2007). The amino acids at the corresponding position of the first protomer in GII.3 were investigated and all found to be ACR; in chronological order: 356 (Thr), 357 (Thr), 358 (Arg) and 386 (Asp) (Fig.…”

Section: Et Analysismentioning

confidence: 99%

“…Each capsid protein is folded into two major domains, the S (shell) and the P (protruding) domains that are connected via an eight aa hinge region. The P domain is further subdivided into P1-1, P1-2 and P2, the last located on the most exterior part of the capsid and therefore predicted to bear antigenic determinants affecting the immunological response and host specificity, including the receptor-binding pocket (Cao et al, 2007;Prasad et al, 1999).…”

Section: Introductionmentioning

confidence: 99%

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Quasispecies dynamics and molecular evolution of human norovirus capsid P region during chronic infection

Carlsson

Lindberg²,

Rodrı́guez-Dı́az

et al. 2009

Journal of General Virology

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In this novel study, we have for the first time identified evolutionarily conserved capsid residues in an individual chronically infected with norovirus (GGII.3). From 2000 to 2003, a total of 147 P1-1 and P2 capsid sequences were sequenced and investigated for evolutionarily conserved and functionally important residues by the evolutionary trace (ET) algorithm. The ET algorithm revealed more absolutely conserved residues (ACR) in the P1-1 domain (47/53, 88 %) as compared with the P2 domain (86/133, 64 %). The capsid P1-1 and P2 domains evolved in time-dependent manner, with a distinct break point observed between autumn/winter of year 2000 (isolates P1, P3 and P5) and spring to autumn of year 2001 (isolates P11, P13 and P15), which presumably coincided with a change of clinical symptoms. Furthermore, the ET analysis revealed a similar receptor-binding pattern as reported for Norwalk and VA387 strains, with the CS-4 and CS-5 patch (Norwalk strain) including residues 329 and 377 and residues 306 and 310, respectively, all being ACR in all partitions. Most interesting was that residues 343, 344, 345, 374, 390 and 391 of the proposed receptor A and B trisaccharide binding site (VA387 strain) within the P2 domain remained ACR in all partitions, presumably because there was no selective advantage to alter the histo blood group antigens (HBGA) receptor binding specificity. In conclusion, this study provides novel insights to the evolutionary process of norovirus during chronic infection.

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Section: Discussionmentioning

confidence: 99%

Section: Et Analysismentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Quasispecies dynamics and molecular evolution of human norovirus capsid P region during chronic infection

Carlsson

Lindberg²,

Rodrı́guez-Dı́az

et al. 2009

Journal of General Virology

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“…Superimposition of P2 and P1 by Dali server yields a Z score of 2.1. P2 is also homologous to the receptor binding domain of norovirus in the Caliciviridae family (Z score ϭ 2.0) (25). Noroviruses use blood-group trisaccharides as cell receptors.…”

Section: Resultsmentioning

confidence: 99%

Structure of the hepatitis E virus-like particle suggests mechanisms for virus assembly and receptor binding

Guu

Liu

et al. 2009

Proc. Natl. Acad. Sci. U.S.A.

223

247

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Hepatitis E virus (HEV), a small, non-enveloped RNA virus in the familyHepeviridae, is associated with endemic and epidemic acute viral hepatitis in developing countries. Our 3.5-Å structure of a HEV-like particle (VLP) shows that each capsid protein contains 3 linear domains that form distinct structural elements: S, the continuous capsid; P1, 3-fold protrusions; and P2, 2-fold spikes. The S domain adopts a jelly-roll fold commonly observed in small RNA viruses. The P1 and P2 domains both adopt ␤-barrel folds. Each domain possesses a potential polysaccharide-binding site that may function in cell-receptor binding. Sugar binding to P1 at the capsid protein interface may lead to capsid disassembly and cell entry. Structural modeling indicates that native T ‫؍‬ 3 capsid contains flat dimers, with less curvature than those of T ‫؍‬ 1 VLP. Our findings significantly advance the understanding of HEV molecular biology and have application to the development of vaccines and antiviral medications.capsid ͉ HEV V iral hepatitis is principally caused by 5 distinct viruses named hepatitis A-E. Despite their similar names, the 5 viruses are unrelated, and they have totally different genome structures with distinct replication mechanisms. Hepatitis E virus (HEV) is responsible for endemic hepatitis as well as sporadic epidemics of acute, enterically transmitted hepatitis in the developing world, including parts of Asia, the Middle East, Africa, and Mexico (1, 2). HEV accounts for more than 50% of acute viral hepatitides in young adults in these regions, with a case fatality of 1-2% in regular patients and up to 20% in pregnant women.Given the lack of a robust cell culture system, and because HEV is not closely related to any other well-characterized virus, little is known about the molecular biology of HEV or its strategy for replication (1). HEV is a small, non-enveloped virus with a 7.2 kb, positive-sense RNA genome. Its genomic RNA is polyadenylated and contains 3 ORFs. Located near the 5Ј-end, ORF1 encodes a non-structural polyprotein with multiple functional domains, including those for methyltransferase, protease, helicase, and polymerase. The viral capsid protein (CP) is encoded by ORF2 near the 3Ј-end. ORF3, which partially overlaps with the other 2 ORFs, codes for an immunogenic protein of unknown function. HEV was originally classified in the Caliciviridae family because of its structural similarity to other caliciviruses; however, it is now the sole member of the Hepeviridae family. The genomic RNA of HEV exhibits several distinct features compared to the genomic RNA of caliciviruses, including a methylated cap at the 5Ј-end and an ORF1 with functional domains arranged in a different order (1, 3).Previous studies of HEV assembly have primarily focused on the overexpression of viral proteins. The ORF2 capsid protein, HEV-CP, contains a total of 660 amino acid residues. At the HEV-CP N terminus is a signal peptide followed by an arginine-rich domain that potentially play a role in viral RNA encapsidation during assem...

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“…The NV protruding (P) domain of the VP1 capsid protein was cocrystallized with certain saccharides of the histo-blood group antigens (HBGAs), following a proposed association of HBGA binding with viral entry into epithelial cells of the gastrointestinal tract (9). The amino acids involved in this interaction were identified, and two sites (interaction sites 1 and 2) that participate in trisaccharide A and B binding were mapped (10,11).…”

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confidence: 99%

Chimpanzees as an animal model for human norovirus infection and vaccine development

Bok

Parra²,

Mitra³

et al. 2010

Proc. Natl. Acad. Sci. U.S.A.

208

196

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Noroviruses are global agents of acute gastroenteritis, but the development of control strategies has been hampered by the absence of a robust animal model. Studies in chimpanzees have played a key role in the characterization of several fastidious hepatitis viruses, and we investigated the feasibility of such studies for the noroviruses. Seronegative chimpanzees inoculated i.v. with the human norovirus strain Norwalk virus (NV) did not show clinical signs of gastroenteritis, but the onset and duration of virus shedding in stool and serum antibody responses were similar to that observed in humans. NV RNA was detected in intestinal and liver biopsies concurrent with the detection of viral shedding in stool, and NV antigen expression was observed in cells of the small intestinal lamina propria. Two infected chimpanzees rechallenged 4, 10, or 24 mo later with NV were resistant to reinfection, and the presence of NV-specific serum antibodies correlated with protection. We evaluated the immunogenicity and efficacy of virus-like particles (VLPs) derived from NV (genogroup I, GI) and MD145 (genogroup II, GII) noroviruses as vaccines. Chimpanzees vaccinated intramuscularly with GI VLPs were protected from NV infection when challenged 2 and 18 mo after vaccination, whereas chimpanzees that received GII VLPs vaccine or a placebo were not. This study establishes the chimpanzee as a viable animal model for the study of norovirus replication and immunity, and shows that NV VLP vaccines could induce protective homologous immunity even after extended periods of time.

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Structural Basis for the Recognition of Blood Group Trisaccharides by Norovirus

Cited by 340 publications

References 32 publications

Quasispecies dynamics and molecular evolution of human norovirus capsid P region during chronic infection

Quasispecies dynamics and molecular evolution of human norovirus capsid P region during chronic infection

Structure of the hepatitis E virus-like particle suggests mechanisms for virus assembly and receptor binding

Chimpanzees as an animal model for human norovirus infection and vaccine development

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